3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase
| 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.107 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase (EC 4.2.1.107) is an enzyme that catalyzes the chemical reaction
- (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O
Thus, the substrate of this enzyme are (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA, whereas its two products are (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA and H2O.
Nomenclature
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase [(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA-forming]. Other names in common use include 46 kDa hydratase 2, and (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase.
References
Further reading
- Qin YM, Haapalainen AM, Conry D, Cuebas DA, Hiltunen JK, Novikov DK (December 1997). "Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal multifunctional enzyme 2: role of the hydratase reaction in bile acid synthesis". The Biochemical Journal. 328 ( Pt 2): 377–82. PMC 1218931. PMID 9371691.
- Xu R, Cuebas DA (April 1996). "The reactions catalyzed by the inducible bifunctional enzyme of rat liver peroxisomes cannot lead to the formation of bile acids". Biochemical and Biophysical Research Communications. 221 (2): 271–8. doi:10.1006/bbrc.1996.0585. PMID 8619845.
- Kokawa NI; Morisaki M (1988). "Synthesis and determination of stereochemistry of four diastereoisomers at the C-24 and C-25 positions of 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid and cholic acid". Chem. Pharm. Bull. 36: 134–141. doi:10.1248/cpb.36.134.
- Sonoda Y; Sato Y; Morisaki M (1988). "Non-stereoselective conversion of the four diastereoisomers at the C-24 and C-25 positions of 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid and cholic acid". Chem. Pharm. Bull. 36: 142–145. doi:10.1248/cpb.36.142.
- Kurosawa T, Sato M, Nakano H, Fujiwara M, Murai T, Yoshimura T, Hashimoto T (February 2001). "Conjugation reactions catalyzed by bifunctional proteins related to beta-oxidation in bile acid biosynthesis". Steroids. 66 (2): 107–14. doi:10.1016/S0039-128X(00)00217-8. PMID 11146090.
- Russell DW (2003). "The enzymes, regulation, and genetics of bile acid synthesis". Annual Review of Biochemistry. 72: 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.